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Cyclic adenosine monophosphate
| Section2 = | Section3 = }} Cyclic adenosine monophosphate (cAMP, cyclic AMP or 3'-5'-cyclic adenosine monophosphate) is a molecule that is important in many biological processes; it is derived from what is known as adenosine triphosphate (ATP). Synthesis and decomposition cAMP is synthesised from ATP by adenylyl cyclase which is located at the cell membranes. Adenylyl cyclase is activated by the hormones glucagon and epinephrine through the activation of adenylyl cyclase stimulatory G (Gs)-coupled receptors and inhibited by agonists of adenylyl cyclase inhibitory G (Gi)-protein coupled receptors. Liver adenylyl cyclase responds more strongly to glucagon, and muscle adenylyl cyclase responds more strongly to adrenaline. cAMP decomposition into AMP is catalyzed by the enzyme phosphodiesterase. Functions cAMP is a second messenger, used for intracellular signal transduction, such as transferring the effects of hormones like glucagon and adrenaline, which cannot get through the cell membrane. Its purposes include the activation of protein kinases and regulating the effects of adrenaline and glucagon. It is also used to regulate the passage of Ca2+ through ion channels. In humans (adrenaline) binds its receptor, that associates with an heterotrimeric G protein. The G protein associates with adenylyl cyclase that converts ATP to cAMP, spreading the signal (more details...)]] In humans, cyclic AMP works by activating protein kinase A (PKA, also known as cAMP-dependent protein kinase). This is normally inactive as a tetrameric holoenzyme, consisting of 2 catalytic and 2 regulatory units (C2R2), with the regulatory units blocking the catalytic centers of the catalytic units. Cyclic AMP binds to specific locations on the regulatory units of the protein kinase, and causes dissociation between the regulatory and catalytic subunits, thus activating the catalytic units and enabling them to phosphorylate substrate proteins. Further effects thus depends on cAMP-dependent protein kinase, which are found in function of cAMP-dependent protein kinase. These effects depend on the type of cell, but includes regulation of glycogen, sugar, and lipid metabolism. Cyclic AMP activates protein kinase A by binding to its two regulatory subunits, causing the release of active catalytic subunits. The active subunits catalyze the transfer of phosphate from ATP to specific serine or threonine residues of protein substrates. The phosphorylated proteins may act directly on the cell's ion channels, or may become activated or inhibited enzymes. Protein kinase A can also phosphorylate specific proteins that bind to promoter regions of DNA, causing increased expression of specific genes. Not all protein kinases respond to cAMP: several types of protein kinases are not cAMP dependent, for example protein kinase C. Pathology Role of cAMP in human carcinoma Some research has suggested that a deregulation of cAMP pathways and an aberrant activation of cAMP-controlled genes is linked to the growth of some cancers.American Association for Cancer Research (cAMP-responsive Genes and Tumor Progression)American Association for Cancer Research (cAMP Dysregulation and Melonoma)American Association for Cancer Research (cAMP-binding Proteins' Presence in Tumors) Role of cAMP in Prefrontal Cortex Disorders Recent research may indicate that cAMP affects the function of higher order thinking in the prefrontal cortex through its regulation of ion channels called hyperpolarization-activated cyclic nucleotide-gated channels (HCN). 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